The Open Protein Structure Annotation Network
PDB Keyword


    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Crystal structure of hypothetical protein (np_422103.1) from Caulobacter crescentus at 1.85 A resolution. To be published
    Site JCSG
    PDB Id 2hbo Target Id 366861
    Molecular Characteristics
    Source Caulobacter crescentus cb15
    Alias Ids TPS1481,NP_422103.1, 382773 Molecular Weight 17419.83 Da.
    Residues 157 Isoelectric Point 5.58
    Sequence msddltdaqtaaipegfsqlnwsrgfgrqigplfehregpgqarlafrveehhtnglgnchggmlmsfa dmawgriislqksyswvtvrlmcdflsgaklgdwvegegeliseedmlftvrgriwagertlitgtgvf kalsarkprpgelaykeea
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.85 Rfree 0.244
    Matthews' coefficent 2.10 Rfactor 0.208
    Waters 64 Solvent Content 41.08

    Ligand Information


    Google Scholar output for 2hbo
    1. Protein fold and structure in the truncated (2/2) globin family
    M Nardini, A Pesce, M Milani, M Bolognesi - Gene, 2007 - Elsevier
    2. Protein structure in the truncated (2/2) hemoglobin family
    A Pesce, M Nardini, M Milani, M Bolognesi - IUBMB life, 2007 - Wiley Online Library
    3. Analysis of proteins with the'hot dog'fold: Prediction of function and identification of catalytic residues of hypothetical proteins
    LS Pidugu, K Maity, K Ramaswamy - BMC structural , 2009 - biomedcentral.com
    4. Ab initio protein structure prediction with force field parameters derived from water_phase quantum chemical calculation
    D Katagiri, H Fuji, S Neya - Journal of computational , 2008 - Wiley Online Library
    5. Reconstruction of Protein Backbone with the alpha-Carbon Coordinates
    JH Wang, CB Yang, CT Tseng - Journal of Information Science , 2010 - etd.lib.nsysu.edu.tw
    6. The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125
    BD Howes, D Giordano, L Boechi, R Russo - Journal of Biological , 2011 - Springer
    7. Structural characterization of a group II 2/2 hemoglobin from the plant pathogen Agrobacterium tumefaciens
    A Pesce, M Nardini, M LaBarre, C Richard - et Biophysica Acta (BBA , 2011 - Elsevier
    8. Reconstruction of Protein Backbone with the a-Carbon Coordinates
    JH Wang, CB Yang, CT Tseng - 2007 - asiair.asia.edu.tw
    9. Refinement of All-atom Backbone Prediction of Proteins
    HY Chang - 2008 - etd.lib.nsysu.edu.tw
    10. Structure and function of hemoproteins from cold-adapted organism
    R Russo - 2011 - fedoa.unina.it
    11. The truncated hemoglobin from Thermobifida fusca
    FP Nicoletti - Resonance Raman Spectroscopy As a Tool To Study , 2010 - unifi.it
    12. Structural and functional studies of hemoproteins from polar marine organisms
    D Coppola - 2011 - fedoa.unina.it

    Protein Summary

    The gene CC_3309 from Caulobacter crescentus encodes the NP_422103 protein, a putative PaaI thioesterase (phenylacetic acid degradation protein), and a member of the thioesterase superfamily PF03061. Genome context analysis shows a predicted functional link (score 0.89) with CC_3308, a putative hydrolase.

    The enzyme belongs to the class of alpha and beta (a+b) proteins and adopts a  thioesterase/thiol ester dehydrase-isomerase (hot-dog) fold type SCOP54636. A DALI structural similarity search reports as top hits the thioesterase PDB:2h4u (Z=16), the phenylacetic acid degradation protein PaaI PDB:1wlv (Z=15), and the hypothetical protein PA5202  PDB:1zki (Z=15). The structures of the enzyme homologues from other organisms have been determined: PDB:2fs2  (Z=14), E. coli; PDB:2dsl (Z=14), Thermus thermophilus.

    The enzyme participates in the aerobic phenylacetate degradation pathway.  This pathway targets a variety of environmental aromatics of natural and synthetic origin.  The enzyme is potentially useful for bioremediation of environmental aromatic pollutants and for chemical synthesis [Ref].  

    Ligand Summary





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